In vitro and in vivo neurotoxicity of prion protein oligomers.

Autor: Steve Simoneau, Human Rezaei, Nicole Salès, Gunnar Kaiser-Schulz, Maxime Lefebvre-Roque, Catherine Vidal, Jean-Guy Fournier, Julien Comte, Franziska Wopfner, Jeanne Grosclaude, Hermann Schätzl, Corinne Ida Lasmézas

Publikováno v: PLoS Pathogens, Vol 3, Iss 8, p e125 (2007)

The mechanisms underlying prion-linked neurodegeneration remain to be elucidated, despite several recent advances in this field. Herein, we show that soluble, low molecular weight oligomers of the full-length prion protein (PrP), which possess charac

Externí odkaz: https://doaj.org/article/b78586e103e84f01b240feec7e8ce3fb

Recognition of Lumenal Prion Protein Aggregates by Post-ER Quality Control Mechanisms Is Mediated by the Preoctarepeat Region of PrP

Autor: Franziska Wopfner, Lajos László, Hermann M. Schätzl, Sabine Gilch, Max Nunziante, Alexa Ertmer

Publikováno v: Traffic. 5:300-313

Prion diseases are fatal transmissible neurodegenerative disorders linked to an aberrant conformation of the cellular prion protein (PrP(c)). We have shown previously that the chemical compound suramin induced aggregation of fully matured PrP(c) in p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::83536e17452db2a05840cfa44bfe6692
https://doi.org/10.1111/j.1600-0854.2004.0175.x

Polyclonal Anti-PrP Auto-antibodies Induced with Dimeric PrP Interfere Efficiently with PrPSc Propagation in Prion-infected Cells

Autor: Ingrid Renner-Müller, Hermann M. Schätzl, Gottfried Brem, Elisabeth Kremmer, Sabine Gilch, Martin H. Groschup, Franziska Wopfner, Christine Bauer, Eckhard Wolf

Publikováno v: J. Biol. Chem. 278, 18524-18531 (2003)

Prion diseases are neurodegenerative infectious disorders for which no prophylactic regimens are known. In order to induce antibodies/auto-antibodies directed against surface-located PrP(c), we used a covalently linked dimer of mouse prion protein ex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf5090dcff4fd030a9efff2c2e6f4f0f
https://doi.org/10.1074/jbc.m210723200

Humoral immune response to native eukaryotic prion protein correlates with anti-prion protection

Autor: Erica C. Pellicioli, Frank L. Heppner, Adriano Aguzzi, Eduard Urich, Burkhard Becher, Hermann M. Schätzl, Gino Miele, Nathalie Braun, Franziska Wopfner, Magdalini Polymenidou

Prion diseases are characterized by the deposition of an abnormal form (termed PrP Sc ) of the cellular prion protein (PrP C ). Because antibodies to PrP C can antagonize deposition of PrP Sc in cultured cells and mice, they may be useful for anti-pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f921d1c79d614e6bb116a65471b27dc8
https://doi.org/10.5167/uzh-1955

In Vitro and In Vivo Neurotoxicity of Prion Protein Oligomers

Autor: Jeanne Grosclaude, Catherine Vidal, Julien Comte, Hermann M. Schätzl, Human Rezaei, Nicole Salès, Franziska Wopfner, Gunnar Kaiser-Schulz, Steve Simoneau, Jean Guy Fournier, Corinne Ida Lasmézas, Maxime Lefebvre-Roque

Publikováno v: PLoS Pathogens
PLoS Pathogens, 2007, 3 (8), pp.1175-1186. ⟨10.1371/journal.ppat.0030125⟩
PLoS Pathogens, Public Library of Science, 2007, 3 (8), pp.1175-1186. ⟨10.1371/journal.ppat.0030125⟩
Plos Pathogens 8 (3), 1175-1186. (2007)
PLoS Pathogens, Vol 3, Iss 8, p e125 (2007)

The mechanisms underlying prion-linked neurodegeneration remain to be elucidated, despite several recent advances in this field. Herein, we show that soluble, low molecular weight oligomers of the full-length prion protein (PrP), which possess charac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40eeb1193d1487ff6a61b6375e5dfa93
https://doi.org/10.1371/journal.ppat.0030125